Structure of PDB 6zn2 Chain E Binding Site BS03
Receptor Information
>6zn2 Chain E (length=335) Species:
9606
(Homo sapiens) [
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VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQ
YRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFS
GYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQ
YIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEE
IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAF
DPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
Ligand information
Ligand ID
FE
InChI
InChI=1S/Fe/q+3
InChIKey
VTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
Formula
Fe
Name
FE (III) ION
ChEMBL
DrugBank
DB13949
ZINC
PDB chain
6zn2 Chain E Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
6zn2
Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Resolution
4.3 Å
Binding residue
(original residue number in PDB)
H330 H335 E375
Binding residue
(residue number reindexed from 1)
H168 H173 E213
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.14.16.2
: tyrosine 3-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497
monooxygenase activity
GO:0005506
iron ion binding
GO:0016714
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072
aromatic amino acid metabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:6zn2
,
PDBe:6zn2
,
PDBj:6zn2
PDBsum
6zn2
PubMed
35013193
UniProt
P07101
|TY3H_HUMAN Tyrosine 3-monooxygenase (Gene Name=TH)
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